INO80_VANPO
ID INO80_VANPO Reviewed; 1556 AA.
AC A7TJI3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=Kpol_534p5;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P53115};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS480402; EDO17526.1; -; Genomic_DNA.
DR RefSeq; XP_001645384.1; XM_001645334.1.
DR AlphaFoldDB; A7TJI3; -.
DR SMR; A7TJI3; -.
DR STRING; 436907.A7TJI3; -.
DR EnsemblFungi; EDO17526; EDO17526; Kpol_534p5.
DR GeneID; 5545748; -.
DR KEGG; vpo:Kpol_534p5; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; A7TJI3; -.
DR OMA; GCQREVK; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR031047; Ino80.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1556
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350965"
FT DOMAIN 572..697
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 812..984
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1381..1535
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 153..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 935..938
FT /note="DEAQ box"
FT COMPBIAS 189..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 825..832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1556 AA; 180155 MW; A6B916E7B577D449 CRC64;
MSLAKLLNND DDDNNINLPN INVNNTNTND TSSSIVTNTH TTNTTTNLQK EKFLNKLNND
FNLLNKRDNL ELNYQDWKFL NYQEFELLNE WNQQSKEWNN SIKNFEYLYS LMKKYKSEWE
NYLTLKSSDK YLKNVVNDCL INSNTNNLKS KSKLKTDTKT KAKSKSKSKL KLKSNSDAKV
KSKSSNAKAK AKTKSVSTQQ KRKRTTSIKN LLEKEDSALT SLDDMDEIDD VNEILNNDNN
DEITQNSKDL STTTATEKKL NTKTSPSKKR KDEVRVAMKK PMTSTPNVKT ENKSKQKSNK
KNIDADDNTY DDNNLINGKD TEELDDIEKA KDLEDNTDIE IEGTNENEDE DEDEDEDEDE
DEEDEEEGEE EEEEEEDEEG VINMIENEDD EDYFAPGKKS GRQNASKVAG EPAAPVPKTP
TTIHSDRERI VRELIKMCNK NKNKKSRKRR FTNSIVTDYN PEENKLIVKV TLKQYHVRKL
KKLINDAKKL REEEEMKLKK SLMKEAENAE ELEGPSSKKK KLNSGTAQNE NGGEQNSEFI
QNTHDLPTYG MQMTLKEAKA IKRHYDNTFF TILKDLARKD SAKMARLVQQ IQSIRATNFK
KNSSVCAREA RKWQQRNFKQ VKDFQTRARR GIREMLNYWK KNEREERDLK KKAEKVAMEQ
ARKEEEDREN VRQAKKLNFL LTQTELYSHF IGSKIKTNEL EGNMKDDEFD ENEDNLMNNI
DLDSTSSVKT DFKTIDFDNE DDDELRRKAA QNASNVLQKS REKTKKFDND TSNGEELNFQ
NPTSLGEVVI EQPSILACTL KEYQLKGLNW LANLYDQGIN GILADEMGLG KTVQSISVLA
HLAEKYNIWG PFLVVTPAST LHNWVNEISK FVPQFKILPY WGNSNDRKIL RRFWDRKNLR
YNKDSPFHVM ITSYQMVVSD TSYLQKMKWQ YMILDEAQAI KSSQSSRWRN LLSFHCRNRL
LLTGTPIQNN MQELWALLHF IMPSLFDSHD EFNDWFSKDI ESHAEANTKL NQQQLRRLHM
ILKPFMLRRV KKNVQSELGD KIEIDVMCDL TQRQAKLYQI LKSQMSTNYD VIENAAGDDD
TGSDQNMINA VMQFRKVCNH PDLFERADVD SPFSFSIFGK SSSLSRDNEP LVDILYSTRN
PITYHLPRLI YNDLILPNYE NDLGLKNKLL NYTFSIFNNE STCKEISRVT GLTYGEIKRV
VHRDLLMNAI HLKEPYSRQT FLEKISVIED NDKTFSDMNF KSNLKLIERS AKLDALSRVT
STGVLNSLLN IKEQVFDNEY YNAISRSYHP NVSSSPVSIQ VLGNRHFSIQ QEEELFKPVI
SKALSEIPAS TQYNMAVEKK IPLHDFPVSG LYPSPLNKSF SSYISMPSMD RFITESAKLK
KLDELLVELK KGDHRVLIYF QMTKMMDLME EYLTYRQYSH IRLDGSSKLE DRRDLVHDWQ
TRPDIFIFLL STRAGGLGIN LTAADTVIFY DSDWNPTIDS QAMDRAHRLG QTRQVTVYRL
LIRGTIEERM RDRAKQKEHV QQVVMEGKTL QKDVKTIESG GDVKAAAAAS TALTTN
